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Volumn 75, Issue 2, 2000, Pages 624-633

The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis

Author keywords

Apoptosis; Caspase 3; Microtubule; Tau

Indexed keywords

CASPASE 3; TAU PROTEIN;

EID: 0033928035     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0750624.x     Document Type: Article
Times cited : (179)

References (48)
  • 1
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • Anderson A. J., Su J. H., and Cotman C. W. (1996) DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 16, 1710-1719.
    • (1996) J. Neurosci. , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 2
    • 0032146775 scopus 로고    scopus 로고
    • Increased production of amyloid precursor protein provides a substrate for caspase-3 in dying motoneurons
    • Barnes N. Y., Li L., Yoshikawa K., Schwartz L. M., Oppenheim R. W., and Milligan C. E. (1998) Increased production of amyloid precursor protein provides a substrate for caspase-3 in dying motoneurons. J. Neurosci. 18, 5869-5880.
    • (1998) J. Neurosci. , vol.18 , pp. 5869-5880
    • Barnes, N.Y.1    Li, L.2    Yoshikawa, K.3    Schwartz, L.M.4    Oppenheim, R.W.5    Milligan, C.E.6
  • 3
    • 0029845397 scopus 로고    scopus 로고
    • Cytosolic proteolysis of τ by cathepsin D in hippocampus following suppression of cathepsins B and L
    • Bednarski E. and Lynch G. (1996) Cytosolic proteolysis of τ by cathepsin D in hippocampus following suppression of cathepsins B and L. J. Neurochem. 67, 1846-1855.
    • (1996) J. Neurochem. , vol.67 , pp. 1846-1855
    • Bednarski, E.1    Lynch, G.2
  • 4
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • Brancolini C, Benedetti M., and Schneider C. (1995) Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J. 14, 5179-5190.
    • (1995) EMBO J. , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Benedetti, M.2    Schneider, C.3
  • 5
    • 0030707519 scopus 로고    scopus 로고
    • Dismantling cell-cell contacts during apoptosis is coupled to caspase-dependent proteolytic cleavage of β-catenin
    • Brancolini C., Lazarevich D., Rodriguez J., and Schneider C. (1997) Dismantling cell-cell contacts during apoptosis is coupled to caspase-dependent proteolytic cleavage of β-catenin. J. Cell Biol. 139, 759-771.
    • (1997) J. Cell Biol. , vol.139 , pp. 759-771
    • Brancolini, C.1    Lazarevich, D.2    Rodriguez, J.3    Schneider, C.4
  • 7
    • 0033636759 scopus 로고    scopus 로고
    • The solution structure of a C-terminal peptide of human tau
    • in press
    • Esposito G., Viglino P., Novak M., and Cattaneo A. (2000) The solution structure of a C-terminal peptide of human tau. J. Pept. Sci. (in press).
    • (2000) J. Pept. Sci.
    • Esposito, G.1    Viglino, P.2    Novak, M.3    Cattaneo, A.4
  • 8
    • 0030463704 scopus 로고    scopus 로고
    • Overexpression of Alzheimer's PHF core tau fragments: Implications for the tau truncation hypothesis
    • Fasulo L., Ovecka M., Kabat J., Bradbury A., Novak M., and Cattaneo A. (1996) Overexpression of Alzheimer's PHF core tau fragments: implications for the tau truncation hypothesis. Alzheimers Res. 2, 195-200.
    • (1996) Alzheimers Res. , vol.2 , pp. 195-200
    • Fasulo, L.1    Ovecka, M.2    Kabat, J.3    Bradbury, A.4    Novak, M.5    Cattaneo, A.6
  • 9
    • 22044447582 scopus 로고    scopus 로고
    • Tau truncation in Alzheimer's disease: Expression of a fragment encompassing PHF core tau induces apoptosis in COS cells
    • Fasulo L., Visintin M., Novak M., and Cattaneo A. (1998) Tau truncation in Alzheimer's disease: expression of a fragment encompassing PHF core tau induces apoptosis in COS cells. Alzheimer's Rep. 1, 25-32.
    • (1998) Alzheimer's Rep. , vol.1 , pp. 25-32
    • Fasulo, L.1    Visintin, M.2    Novak, M.3    Cattaneo, A.4
  • 10
    • 0032426430 scopus 로고    scopus 로고
    • Caspase-3-induced gelsolin fragmentation contributes to actin cytoskeletal collapse, nucleolysis, and apoptosis of vascular smooth muscle cells exposed to proinflammatory cytokines
    • Geng Y. J., Azuma T., Tang J. X., Hartwig J. H., Muszynski M., Wu Q., Libby P., and Kwiatkowski D. J. (1998) Caspase-3-induced gelsolin fragmentation contributes to actin cytoskeletal collapse, nucleolysis, and apoptosis of vascular smooth muscle cells exposed to proinflammatory cytokines. Eur. J. Cell. Biol. 77, 294-302.
    • (1998) Eur. J. Cell. Biol. , vol.77 , pp. 294-302
    • Geng, Y.J.1    Azuma, T.2    Tang, J.X.3    Hartwig, J.H.4    Muszynski, M.5    Wu, Q.6    Libby, P.7    Kwiatkowski, D.J.8
  • 12
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M., Spillantini M. G., Cairns N. J., and Crowther R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 14
    • 0029658187 scopus 로고    scopus 로고
    • Bcl-xL overexpression inhibits Taxol-induced Yama protease activity and apoptosis
    • Ibrado A. M., Huang Y., Fang G., and Bhalla K. (1996) Bcl-xL overexpression inhibits Taxol-induced Yama protease activity and apoptosis. Cell Growth Differ. 71, 1087-1094.
    • (1996) Cell Growth Differ. , vol.71 , pp. 1087-1094
    • Ibrado, A.M.1    Huang, Y.2    Fang, G.3    Bhalla, K.4
  • 16
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • Janicke R. U., Ng P., Sprengart M. L., and Porter A. G. (1998) Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J. Biol. Chem. 273, 15540-15545.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15540-15545
    • Janicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 17
    • 0031025396 scopus 로고    scopus 로고
    • The τ protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments
    • Johnson G. V., Seubert P., Cox T. M., Motter R., Brown J. P., and Galasko D. (1997) The T protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. J. Neurochem. 68, 430-433.
    • (1997) J. Neurochem. , vol.68 , pp. 430-433
    • Johnson, G.V.1    Seubert, P.2    Cox, T.M.3    Motter, R.4    Brown, J.P.5    Galasko, D.6
  • 18
    • 0029876247 scopus 로고    scopus 로고
    • Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition
    • Kayalar C., Ord T., Testa M. P., Zhong L. T., and Bredesen D. E. (1996) Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition. Proc. Natl. Acad. Sci. USA 93, 2234-2238.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2234-2238
    • Kayalar, C.1    Ord, T.2    Testa, M.P.3    Zhong, L.T.4    Bredesen, D.E.5
  • 19
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim T. W., Pettingell W. H., Jung Y. K., Kovacs D. M., and Tanzi R. E. (1997) Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277, 373-376.
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 21
    • 0028981717 scopus 로고
    • The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LeFerla F. M., Tinkle B. T., Bieberich C. J., Haudenschild C. C., and Jay G. (1995) The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat. Genet. 9, 21-30.
    • (1995) Nat. Genet. , vol.9 , pp. 21-30
    • LeFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 27
    • 0030693292 scopus 로고    scopus 로고
    • Cell and molecular neurobiology of presenilins: A role for the endoplasmic reticulum in the pathogenesis of Alzheimer's disease?
    • Mattson M. P. and Guo Q. (1997) Cell and molecular neurobiology of presenilins: a role for the endoplasmic reticulum in the pathogenesis of Alzheimer's disease? J. Neurosci. Res. 50, 505-513.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 505-513
    • Mattson, M.P.1    Guo, Q.2
  • 28
    • 0029039987 scopus 로고
    • Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau
    • Mercken M., Grynspan F., and Nixon R. A. (1995) Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau. FEBS Lett. 368, 10-14.
    • (1995) FEBS Lett. , vol.368 , pp. 10-14
    • Mercken, M.1    Grynspan, F.2    Nixon, R.A.3
  • 29
    • 0029791355 scopus 로고    scopus 로고
    • Huntington disease: New insights into the relationship between CAG expansion and disease
    • Nasir J., Goldberg Y. P., and Hayden M. R. (1996) Huntington disease: new insights into the relationship between CAG expansion and disease. Hum. Mol. Genet. 5, 1431-1435.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1431-1435
    • Nasir, J.1    Goldberg, Y.P.2    Hayden, M.R.3
  • 30
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • Novak M., Jakes R., Edwards P. C., Milstein C., and Wischik C. M. (1991) Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc. Natl. Acad. Sci. USA 88, 5837-5841.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 31
    • 0027398169 scopus 로고
    • Molecular characterisation of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M., Kabat J., and Wischik C. M. (1993) Molecular characterisation of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 12, 365-370.
    • (1993) EMBO J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 33
    • 0029072690 scopus 로고
    • Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models
    • Portera-Cailliau C., Hedreen J. C., Price D. L., and Koliatsos V. E. (1995) Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models. J. Neurosci. 15, 3775-3787.
    • (1995) J. Neurosci. , vol.15 , pp. 3775-3787
    • Portera-Cailliau, C.1    Hedreen, J.C.2    Price, D.L.3    Koliatsos, V.E.4
  • 35
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signalling by proteolysis
    • Salvesen G. S. and Dixit V. M. (1997) Caspases: intracellular signalling by proteolysis. Cell 91, 443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 36
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I., Xu C. J., Juo P., Kakizaka A., Blenis J., and Yuan J. (1999) Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22, 623-633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 38
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Schweers O., Mandelkow E. M., Biernat J., and Mandelkow E. (1995) Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc. Natl. Acad. Sci. USA 92, 8463-8467.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 39
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini M. G. and Goedert M. (1998) Tau protein pathology in neurodegenerative diseases. Trends Neurosci. 21, 428-433.
    • (1998) Trends Neurosci. , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 40
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L. T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D. R., Poirier G. G., Salvesen G. S., and Dixit V. M. (1995) Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81, 801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 41
    • 0031450192 scopus 로고    scopus 로고
    • Co-localisation of truncated tau and DNA fragmentation in Alzheimer's disease neurones
    • Ugolini G., Cattaneo A., and Novak M. (1997) Co-localisation of truncated tau and DNA fragmentation in Alzheimer's disease neurones. Neuroreport 8, 3709-3712.
    • (1997) Neuroreport , vol.8 , pp. 3709-3712
    • Ugolini, G.1    Cattaneo, A.2    Novak, M.3
  • 43
    • 0033605252 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases
    • Weidemann A., Paliga K., Durrwang U., Reinhard F. B., Schuckert O., Evin G., and Masters C. L. (1999) Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases. J. Biol. Chem. 274, 5823-5829.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5823-5829
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3    Reinhard, F.B.4    Schuckert, O.5    Evin, G.6    Masters, C.L.7
  • 46
    • 0030042249 scopus 로고    scopus 로고
    • Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype
    • Yamatsuji T., Okamoto T., Takeda S., Murayama Y., Tanaka N., and Nishimoto I. (1996) Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype. EMBO J. 15, 498-509.
    • (1996) EMBO J. , vol.15 , pp. 498-509
    • Yamatsuji, T.1    Okamoto, T.2    Takeda, S.3    Murayama, Y.4    Tanaka, N.5    Nishimoto, I.6
  • 48
    • 0033145416 scopus 로고    scopus 로고
    • Caspase activity sows the seeds of neuronal death
    • Yuan J. and Yankner B. A. (1999) Caspase activity sows the seeds of neuronal death. Nat. Cell. Biol. 1, E44-E45.
    • (1999) Nat. Cell. Biol. , vol.1
    • Yuan, J.1    Yankner, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.